Translocation of protein kinase C in rat islets of Langerhans. Effects of a phorbol ester, carbachol and glucose

FEBS Lett. 1989 Mar 13;245(1-2):80-4. doi: 10.1016/0014-5793(89)80196-6.

Abstract

In unstimulated rat islets (2 mM glucose), most of the ion-exchange purified protein kinase C (PKC) activity was associated with the cytosolic fraction. Both carbachol and phorbol myristate acetate caused a significant translocation of PKC activity from cytosolic to membrane fractions, but under the same conditions, glucose (20 mM) did not cause such a redistribution of PKC activity. PMA-induced translocation of PKC to the membrane fraction was also observed in electrically permeabilised islets, in which recovery of the enzyme activity was enhanced by buffering the intracellular Ca2+ concentration to 50 nM and supplying the permeabilised islets with protease inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbachol / pharmacology*
  • Cell Membrane / metabolism
  • Cell Membrane Permeability
  • Cytosol / metabolism
  • Female
  • Glucose / pharmacology*
  • Islets of Langerhans / drug effects
  • Islets of Langerhans / enzymology*
  • Male
  • Protein Kinase C / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • Carbachol
  • Protein Kinase C
  • Glucose
  • Tetradecanoylphorbol Acetate